Macromolecular organization of basement membranes

Current Opinion in Cell Biology

Volumn 8, Issue 5, 1996, Pages 618-624

  Timpl, Rupert ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AGRIN; CELL RECEPTOR; COLLAGEN TYPE 4; ENTACTIN; FIBULIN; ISOPROTEIN; LAMININ; MEMBRANE PROTEIN; OSTEONECTIN; PERLECAN; RECOMBINANT PROTEIN;

BASEMENT MEMBRANE; BINDING SITE; MEMBRANE STRUCTURE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE; REVIEW; STRUCTURE ACTIVITY RELATION;

EID: 0030271572     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80102-5     Document Type: Article

References (60)

1. Timpl R, Brown J: Supramolecular assembly of basement membranes. Bioessays 1996, 18:123-132.
2. Ekblom P, Timpl R (Eds): The Laminins. Reading: Harwood Academic Publisher; 1996.
3. Dziadek M: Role of laminin-nidogen complexes in basement membrane formation during embryonic development Experientia 1995, 51:901-913. A comprehensive review of the mesenchymal origin of nidogen in the assembly of most basement membranes.
4. Simon-Assmann P, Kedinger M, DeArcangelis A, Rousseau V, Simo P: Extracellular matrix components in intestinal development Experientia 1995, 51:883-900. Summary of work on the dependence of the formation of epithelial basement membranes on cell cooperation.
5. Galliano M-F, Aberdam D, Aguzzi A, Ortonne JP, Meneguzzi G: Cloning and complete primary structure of the mouse laminin α3 chain. Distinct expression pattern of the laminin α3A and α3B chain isoforms. J Biol Chem 1995, 270:21820-21826. Identifies two laminin variants resulting from alternative splicing which vary in their short-arm structures, and a novel unknown protein module at the amino terminus of laminin α3B.
6. livanainen A, Sainio K, Sariola H, Tryggvason K: Primary structure and expression of a novel human α4 chain. FEBS Lett 1995, 365:183-188.
7. Miner JH, Lewis RM, Sanes JR: Molecular cloning of a novel laminin chain, α5, and wide spread expression in adult mouse tissues. J Biol Chem 1995, 270:28523-28526. The mammalian laminin α5 chain is a strict homologue of the Drosophila laminin a chain.
8. Airenne T, Haakana H, Sainio K, Kallunki P, Sariola H, Tryggvason K: Structure of the human laminin γ2 chain gene (LAMC2): alternative splicing with different tissue distribution of two transcripts. Genomics 1996, 32:54-64.
9. Matsui C, Wang CK, Nelson CF, Bauer EA, Hoeffler WK: The assembly of laminin-5 subunits. J Biol Chem 1995, 270:23496-23503.
10. Champliaud M-F, Lunstrum GP, Rousselle P, Nishiyama T, Keene DR, Burgeson RE: Human amnion contains a novel laminin variant, laminin 7, which like laminin 6, covalentiy associates with laminin 5 to promote stable epithelial-stromal attachment J Cell Biol 1996, 132:1189-1198.
11. Kammerer R, Antonsson P, Schulthess T, Fauser C, Engel J: Selective chain recognition in the C-terminal α-helical coiled-coil region of laminin. J Mol Biol 1995, 250:64-73.
12. Nomizu M, Utani A, Beck K, Otaka A, Roller PP, Yamada Y: Mechanism of laminin chain assembly into a triple-stranded coiled-coil structure. Biochemistry 1996, 35:2885-2893.
13. Tsen G, Halfter W, Kröger S, Cole GJ: Agrin is a heparan sulfate proteoglycan. J Biol Chem 1995, 270:3392-3399.
14. Denzer AJ, Gesemann M, Schumacher B, Ruegg MA: An amino-terminal extension is required for the secretion of chick agrin and its binding to extracellular matrix. J Cell Biol 1995, 131:1547-1560. Identifies the amino-terminal sequence of agrin and its role in matrix assembly.
15. Kroger S, Norton SE, Honig LS: The developing avian retina expresses agrin isoforms during synaptogenesis. J Neumbiol 1996,29:165-182.
16. Kroger S, Mann S: Biochemical and functional characterization of basal lamina-bound agrin in the chick central nervous system. Eur J Neurosci 1996, 8:500-509.
17. Gesemann MA, Denzer J, Ruegg MA: Acetylcholine receptor-aggregating activity of agrin isoforms and mapping of the active site. J Cell Biol 1995, 128:625-636. This study restricts the basic acetylcholine receptor clustering site of agrin to a single LG module and a single splice site. Cooperation with a second LG module is required for high activity.
18. Couchman JR, Kapoor R, Sthanam M, Wu R-R: Perlecan and basement membrane-chondroitin sulfate proteoglycan (bamacan) are two basement membrane chondroittn/dermatan sulfate proteoglycans in the Engelbreth-Holm-Swarm tumor matrix. J Biol Chem 1996, 271:9595-9602.
19. Muragaki Y, Timmons G, Griffith CM, Oh SP, Fadel B, Quertermous T, Olsen BR: Mouse CoM 8a1 is expressed in a tissue-specific manner as three alternative variants and is localized in basement membrane zones. Proc Natl Acad Sci USA 1995, 92:8763-8767.
20. Brown JC, Timpl R: The collagen superfamily. Int Arch Allergy Immunol 1995, 107:484-490.
21. Mayer U, Zimmermann K, Mann K, Reinhardt D, Timpl R, Mischt R: Binding properties and protease stability of recombinant human nidogen. Eur J Biochem 1995, 227:681-686.
22. Sasaki T, Kostka G, Göhring W, Wiedemann H, Mann K, Chu ML, Timpl R: Structural characterization of two variants of fibulin-1 that differ in nidogen affinity. J Mol Biol 1995, 245:241-250. This paper demonstrates a large difference in nidogen binding by fibulin-1 that is regulated by alternative splicing of the carboxy-terminal domain of fibulin-1.
23. Sasaki T, Göhring W, Pan TC, Chu ML, Timpl R: Binding of mouse and human fibulin-2 to extracellular matrix ligands. J Mol Biol 1995, 254:892-899. This study provides evidence for competition between laminin and fibulin-2 for nidogen binding; this competition could provide a regulatory mechanism in basement membrane assembly.
24. Maurer P, Hohenadl C, Hohenester E, Göhring W, Timpl R, Engel J: The C-terminal portion of BM-40 (SPARC/osteonectm) is an autonomously folding and crystallisable domain that binds calcium and collagen IV. J Mol Biol 1995, 253:347-357.
25. Chakravarti S, Horchar T, Jefferson B, Laurie GW, Hassell JR: Recombinant domain III of perlecan promotes cell attachment through its RGDS sequence. J Biol Chem 1995, 270:404-409.
26. Schulze B, Mann K, Battistutta R, Wiedemann H, Timpl R: Structural properties of recombinant domain III-3 of perlecan containing a globular domain inserted into an epidermalgrowth-factor-like motif. Eur J Biochem 1995, 231:551-556.
27. Schulze B, Sasaki T, Costell M, Mann K, Timpl R: Structural and cell-adhesive properties of three recombinant fragments derived from perlecan domain III. Matrix Biol 1996, in press.
28. Colognato-Pyke H, ORear JJ, Yamada Y, Carbonetto S, Cheng YS, Yurchenco PD: Mapping of network-forming, heparin-binding, and α1β1 integrin-recognition sites within the α-chain short arm of laminin-1. J Biol Chem 1995, 270:9398-9406. Describes the mapping of three binding activities to the amino-terminal LN module of the laminin α1 chain.
29. Schulze B, Mann K, Pöschl E, Yamada Y, Timpl R: Structural and functional analysis of the globular domain IVa of the laminin α1 chain and its impact on an adjacent RGD site. Biochem J 1996, 314:847-851.
30. c-catalyzed modification. J Biol Chem 1995, 270:23415-23420. Describes the identification, by site-directed mutagenesis, of two amine acceptor sites of BM-40 that are involved in covalent cross-linking.
31. 2+-binding module in BM-40. Nat Struct Biol 1996, 3:67-73. The crystal structure of an extracellular calcium binding module in BM-40 reveals the presence of two EF hands which would not be readily predicted from their sequence. This is more comprehensively discussed in another contribution to this issue (see Maurer, Hohenester and Engel, this issue, pp 609-617).
32. Tran H, Tanaka A, Lrtumovich SV, Medved LV, Haudenschild CC, Argraves WS: The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosis. J Biol Chem 1995, 270:19458-19464.
33. Narindrasorasak S, Altman RA, Gonzales-DeWhitt P, Greenberg BD, Kisilevsky R: The interaction between basement membrane and Alzheimer amyloid precursor proteins suggests a role in the pathogenesis of Alzheimer's disease. Lab Invest 1995, 72:272-282.
34. Ries A, Engel J, Lustig A, Kühn K: The function of the NC1 domains in type IV collagen. J Biol Chem 1995, 270:23790-23794.
35. Martin PT, Ettinger AJ, Sanes JR: A synaptic localization domain in the synaptic cleft protein laminin β2 (s-laminin). Science 1995,269:413-416. An elegant study of laminin β1-β2 chain chimeras that localizes their signals for synaptic or extrasynaptic localization to different domains on each chain.
36. Stetefeld J, Mayer U, Timpl R, Huber R: Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin γ1 chain harboring the nidogen binding site. J Mol Biol 1996, 257:644-657. Describes the first analysis by X-ray crystallography of the conformation, disulphide-bond pattern and interface contacts of laminin LE modules. This study also provides the three-dimensional structure of a high-affinity nidogen-binding epitope.
37. Baumgartner R, Czisch M, Mayer U, Pöschl E, Huber R, Timpl R, Holak TA: Structure of nidogen binding LE module of the laminin γ1 chain in solution. J Mol Biol 1996, 257:658-668. The study demonstrates the low conformational flexibility of laminin LE modules, including the nidogen-binding epitope, in solution.
38. Pöschl E, Fox JW, Block D, Mayer U, Timpl R: Two non-contiguous regions contribute to nidogen binding to a single EGF-like motif of the laminin γ1 chain. EMBO J 1994, 13:3741-3747.
39. Mayer U, Pöschl E, Gerecke DR, Wagman DW, Burgeson RE, Timpl R: Low nidogen affinity of laminin-5 can be attributed to two serine residues in EGF-like motif 2III4. FEBS Lett 1995, 536:129-132. Site-directed mutagenesis provides an explanation as to why the laminin γ2 chain does not bind nidogen.
40. Dong U, Hsieh JC, Chung AE: Two distinct cell attachment sites in entactin are revealed by amino acid substitutions and deletion of the RGD sequence in the cysteine-rich epidermal growth factor repeat 2. J Biol Chem 1995, 270:15838-15843.
41. Nomizu M, Kim WH, Yamamura K, Utani A, Song SY, Otaka A, Roller PP, Kleinman HK, Yamada Y: Identification of cell binding sites in the laminin α1 chain carboxy-terminal globular domain by systematic screening of synthetic peptides. J Biol Chem 1995, 270:20583-20590.
42. Underwood PA, Bennett FA, Kirkpatrick A, Bean PA, Moss PA: Evidence for the location of a binding sequence for the α2β1 integrin of endothelial cells, in the β1 subunit of laminin. Biochem J 1995, 309:765-771.
43. Pattaramalai S, Skubitz KM, Skubitz APN: A novel recognition site on laminin for the α2β1 integrin. Exp Cell Res 1996, 222:281-290.
44. Porter BE, Weis J, Sanes JR: A motoneuron-selective stop signal in the synaptic protein s-laminin. Neuron 1995, 14:549-559.
45. Brancaccio A, Schulthess T, Gesemann M, Engel J: Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan. FEBS Lett 1995, 368:139-142.
46. Pall EA, Bolton KM, Ervasti JM: Differential heparin inhibition of skeletal muscle α-dystroglycan binding to laminins. J Biol Chem 1996, 271:3817-3821.
47. Hopf C, Hoch W: Agrin binding to a-dystroglycan. Domains of agrin necessary to induce acetylcholine receptor clustering are overlapping but not identical to the α-dystroglycan-binding region. J Biol Chem 1996, 271:5231-5236. Describes the mapping of three distinct functional activities of agrin to distinct regions of its carboxy-terminal globular domain.
48. Smalheiser NR, Kim E: Purification of cranin, a laminin binding membrane protein. Identity with dystroglycan and reassessment of its carbohydrate moieties. J Biol Chem 1995, 270:15425-15433.
49. Whitelock JM, Murdoch AD, lozzo RV, Underwood PA: The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin and heparanases. J Biol Chem 1996, 271:10079-10086.
50. Noakes PG, Gautam M, Mudd J, Sanes JR, Merlie JP: Aberrant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin β2. Nature 1995, 374:258-262. See annotation [51].
51. Noakes PG, Miner JH, Gautam M, Cunningham JM, Sanes JR, Merlie JP: The renal glomerulus of mice lacking s-laminin/lamlnin β2: nephrosis despite molecular compensation by laminin β1. Nat Genet 1995, 10:400-406. A comprehensive histological, functional and pathological analysis of mice lacking an active laminin β2 chain gene. This deficiency defines distinct biological roles for laminins containing the β2 chain and indicates the existence of compensatory mechanisms. See also [50].
52. De Arcangelis A, Neuville P, Boukamel R, Lefebvre O, Kedinger M, Simon-Assmann P: Inhibition of laminin α1 chain expression leads to alteration of basement membrane assembly and cell differentiation. J Cell Biol 1996, 133:417-430.
53. Xu H, Christmas P, Wu X-R, Wewer UM, Engvall E: Defective muscle basement membrane and lack of M-laminin in the dystrophic dy/dy mouse. Proc Natl Acad Sci USA 1994, 91:5572-5576.
54. Sunada Y, Bernier SM, Kozak CA, Yamada Y, Campbell KP: Deficiency of merosin in dystrophic cry mice and genetic linkage of laminin M chain gene to dy locus. J Biol Chem 1994, 269:13729-13732.
55. Vilquin J-T, Kinoshita I, Roy B, Goulet M, Engvall E, Tome F, Fardeau M, Tremblay JP: Partial laminin α2 chain restoration in α2 chain-deficient dy/dy mouse by primary muscle cell culture transplanation. J Cell Biol 1996, 133:185-197.
56. Xu H, Wu X-R, Wewer UM, Engvall E: Murine muscular dystrophy caused by a mutation in the laminin α2 (Lama2) gene. Nat Genet 1995, 8:297-302. A deletion in the LN module which is involved in self-assembly of the laminin α2 chain does not block synthesis and deposition of the protein but does lead to a severe muscular dystrophy.
57. Helbling-Leclerc A, Zhang X, Topaloglu H, Cruaud C, Tesson F, Weissenbach J, Tome FMS, Schwartz K, Fardeau M, Tryggvason K, Guicheney P: Mutations in the laminin α2-chain gene (LAMA2) cause merosin-deficient congenital muscular dystrophy. Nat Genet 995, 11:216-218.
58. Vidai F, Baudoin C, Miquel C, Galliano M-F, Christiane AM, Uitto J, Ortonne JP, Meneguzzi G: Cloning of the laminin α3 chain gene (LAMA3) and identification of a homozygous deletion in a patient with Herlitz junctional epidermolysis bullosa. Genomics 1995,30:273-280.
59. Iozzo R, Cohen IR, Grässel S, Murdoch AD: The biology of perlecan: the multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices. Biochem J 1994, 302:625-639.
60. Pöschl E, Mayer U, Stetefeld J, Baumgartner R, Holak TA, Huber R, Timpl R: Site-directed mutagenesis and structural interpretation of the nidogen binding site of laminin γ1 chain. EMBO J 1996, in press. Describes a comprehensive epitope mapping by means of 17 point mutations. Together with X-ray crystallography, these results allow us to distinguish between residues of laminin γ1 that are critical for direct binding contacts and those that are important for conformational stabilization.